RCC2_HUMAN - dbPTM
RCC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RCC2_HUMAN
UniProt AC Q9P258
Protein Name Protein RCC2
Gene Name RCC2
Organism Homo sapiens (Human).
Sequence Length 522
Subcellular Localization Nucleus, nucleolus. Chromosome, centromere. Cytoplasm, cytoskeleton, spindle. Appears in the nucleus at G2, then concentrates at the inner centromere region of chromosomes during prophase. Redistributes to the midzone of the mitotic spindle during an
Protein Description Required for completion of mitosis and cytokinesis. May function as a guanine nucleotide exchange factor for the small GTPase RAC1..
Protein Sequence MPRKKAAAAAWEEPSSGNGTARAGPRKRGGPAGRKRERPERCSSSSGGGSSGDEDGLELDGAPGGGKRAARPATAGKAGGAAVVITEPEHTKERVKLEGSKCKGQLLIFGATNWDLIGRKEVPKQQAAYRNLGQNLWGPHRYGCLAGVRVRTVVSGSCAAHSLLITTEGKLWSWGRNEKGQLGHGDTKRVEAPRLIEGLSHEVIVSAACGRNHTLALTETGSVFAFGENKMGQLGLGNQTDAVPSPAQIMYNGQPITKMACGAEFSMIMDCKGNLYSFGCPEYGQLGHNSDGKFIARAQRIEYDCELVPRRVAIFIEKTKDGQILPVPNVVVRDVACGANHTLVLDSQKRVFSWGFGGYGRLGHAEQKDEMVPRLVKLFDFPGRGASQIYAGYTCSFAVSEVGGLFFWGATNTSRESTMYPKAVQDLCGWRIRSLACGKSSIIVAADESTISWGPSPTFGELGYGDHKPKSSTAAQEVKTLDGIFSEQVAMGYSHSLVIARDESETEKEKIKKLPEYNPRTL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
4Methylation----MPRKKAAAAAW
----CCCHHHHHHHC		40.67115980087
5Sumoylation---MPRKKAAAAAWE
---CCCHHHHHHHCC		44.53-
5Sumoylation---MPRKKAAAAAWE
---CCCHHHHHHHCC		44.53-
5Ubiquitination---MPRKKAAAAAWE
---CCCHHHHHHHCC		44.53-
15PhosphorylationAAAWEEPSSGNGTAR
HHHCCCCCCCCCCCC		54.9125159151
16PhosphorylationAAWEEPSSGNGTARA
HHCCCCCCCCCCCCC		47.1725159151
20PhosphorylationEPSSGNGTARAGPRK
CCCCCCCCCCCCCCC		19.5725159151
22MethylationSSGNGTARAGPRKRG
CCCCCCCCCCCCCCC		39.66115389087
27UbiquitinationTARAGPRKRGGPAGR
CCCCCCCCCCCCCCC		59.53-
28MethylationARAGPRKRGGPAGRK
CCCCCCCCCCCCCCC		57.4954559913
43PhosphorylationRERPERCSSSSGGGS
CCCCCHHCCCCCCCC		39.2027273156
44PhosphorylationERPERCSSSSGGGSS
CCCCHHCCCCCCCCC		31.9522167270
45PhosphorylationRPERCSSSSGGGSSG
CCCHHCCCCCCCCCC		19.3922167270
46PhosphorylationPERCSSSSGGGSSGD
CCHHCCCCCCCCCCC		43.3222167270
50PhosphorylationSSSSGGGSSGDEDGL
CCCCCCCCCCCCCCC		34.1322167270
51PhosphorylationSSSGGGSSGDEDGLE
CCCCCCCCCCCCCCC		54.2422167270
74PhosphorylationKRAARPATAGKAGGA
CCCCCCCCCCCCCCE		38.33-
77UbiquitinationARPATAGKAGGAAVV
CCCCCCCCCCCEEEE		41.20-
77AcetylationARPATAGKAGGAAVV
CCCCCCCCCCCEEEE		41.2025953088
772-HydroxyisobutyrylationARPATAGKAGGAAVV
CCCCCCCCCCCEEEE		41.20-
91PhosphorylationVITEPEHTKERVKLE
EECCCCHHCCCEEEC		32.70-
92SumoylationITEPEHTKERVKLEG
ECCCCHHCCCEEECC		45.49-
92SumoylationITEPEHTKERVKLEG
ECCCCHHCCCEEECC		45.4919608861
922-HydroxyisobutyrylationITEPEHTKERVKLEG
ECCCCHHCCCEEECC		45.49-
92AcetylationITEPEHTKERVKLEG
ECCCCHHCCCEEECC		45.4919608861
92UbiquitinationITEPEHTKERVKLEG
ECCCCHHCCCEEECC		45.4921906983
96SumoylationEHTKERVKLEGSKCK
CHHCCCEEECCCCCC		47.22-
96SumoylationEHTKERVKLEGSKCK
CHHCCCEEECCCCCC		47.22-
96AcetylationEHTKERVKLEGSKCK
CHHCCCEEECCCCCC		47.2223749302
120UbiquitinationNWDLIGRKEVPKQQA
CHHHHCCCCCCHHHH		58.83-
124UbiquitinationIGRKEVPKQQAAYRN
HCCCCCCHHHHHHHH		61.28-
124AcetylationIGRKEVPKQQAAYRN
HCCCCCCHHHHHHHH		61.28-
1242-HydroxyisobutyrylationIGRKEVPKQQAAYRN
HCCCCCCHHHHHHHH		61.28-
142PhosphorylationNLWGPHRYGCLAGVR
CCCCCHHCCCCCCCE		14.7920068231
152PhosphorylationLAGVRVRTVVSGSCA
CCCCEEEEEEECCCH		23.5420068231
155PhosphorylationVRVRTVVSGSCAAHS
CEEEEEEECCCHHCE		22.2020068231
157PhosphorylationVRTVVSGSCAAHSLL
EEEEEECCCHHCEEE		7.9620068231
162PhosphorylationSGSCAAHSLLITTEG
ECCCHHCEEEEEECC		21.8320068231
166PhosphorylationAAHSLLITTEGKLWS
HHCEEEEEECCCCCE		20.8220068231
167PhosphorylationAHSLLITTEGKLWSW
HCEEEEEECCCCCEE		35.4320068231
170UbiquitinationLLITTEGKLWSWGRN
EEEEECCCCCEECCC		40.32-
176MethylationGKLWSWGRNEKGQLG
CCCCEECCCCCCCCC		41.71115918345
179UbiquitinationWSWGRNEKGQLGHGD
CEECCCCCCCCCCCC		56.35-
1882-HydroxyisobutyrylationQLGHGDTKRVEAPRL
CCCCCCCCCCCHHHH		60.22-
200PhosphorylationPRLIEGLSHEVIVSA
HHHHHCCCHHHHHEE		28.58-
209GlutathionylationEVIVSAACGRNHTLA
HHHHEEECCCCCEEE		5.4222555962
276PhosphorylationMDCKGNLYSFGCPEY
EECCCCEEEECCCCC		13.1228152594
277PhosphorylationDCKGNLYSFGCPEYG
ECCCCEEEECCCCCC		20.5228152594
283PhosphorylationYSFGCPEYGQLGHNS
EEECCCCCCCCCCCC		8.7025839225
290PhosphorylationYGQLGHNSDGKFIAR
CCCCCCCCCCCCEEE		41.91-
293UbiquitinationLGHNSDGKFIARAQR
CCCCCCCCCEEEEEE		38.2919608861
293MethylationLGHNSDGKFIARAQR
CCCCCCCCCEEEEEE		38.2923583077
293AcetylationLGHNSDGKFIARAQR
CCCCCCCCCEEEEEE		38.2919608861
318UbiquitinationRVAIFIEKTKDGQIL
EEEEEEEECCCCCEE		56.93-
318AcetylationRVAIFIEKTKDGQIL
EEEEEEEECCCCCEE		56.9325953088
319PhosphorylationVAIFIEKTKDGQILP
EEEEEEECCCCCEEC		22.90-
320UbiquitinationAIFIEKTKDGQILPV
EEEEEECCCCCEECC		71.5721906983
320AcetylationAIFIEKTKDGQILPV
EEEEEECCCCCEECC		71.5723749302
342PhosphorylationVACGANHTLVLDSQK
ECCCCCCEEEEECCC		20.5422817900
347PhosphorylationNHTLVLDSQKRVFSW
CCEEEEECCCEEEEE		33.1817525332
349AcetylationTLVLDSQKRVFSWGF
EEEEECCCEEEEECC		55.2525953088
349UbiquitinationTLVLDSQKRVFSWGF
EEEEECCCEEEEECC		55.25-
3492-HydroxyisobutyrylationTLVLDSQKRVFSWGF
EEEEECCCEEEEECC		55.25-
359PhosphorylationFSWGFGGYGRLGHAE
EEECCCCCCCCCCHH		10.2328152594
368UbiquitinationRLGHAEQKDEMVPRL
CCCCHHHHHCHHHHH		47.3521906983
368AcetylationRLGHAEQKDEMVPRL
CCCCHHHHHCHHHHH		47.3523749302
371SulfoxidationHAEQKDEMVPRLVKL
CHHHHHCHHHHHHHH		7.8321406390
377UbiquitinationEMVPRLVKLFDFPGR
CHHHHHHHHHCCCCC		48.2921906983
377AcetylationEMVPRLVKLFDFPGR
CHHHHHHHHHCCCCC		48.2919608861
420PhosphorylationTSRESTMYPKAVQDL
CCCCCCCCHHHHHHH		11.1528102081
422UbiquitinationRESTMYPKAVQDLCG
CCCCCCHHHHHHHHH		43.64-
422AcetylationRESTMYPKAVQDLCG
CCCCCCHHHHHHHHH		43.6423749302
428S-palmitoylationPKAVQDLCGWRIRSL
HHHHHHHHHHHEEEC		7.0829575903
456PhosphorylationSTISWGPSPTFGELG
CCCCCCCCCCCCCCC		32.4121082442
458PhosphorylationISWGPSPTFGELGYG
CCCCCCCCCCCCCCC		48.9221082442
464PhosphorylationPTFGELGYGDHKPKS
CCCCCCCCCCCCCCC		31.8221082442
468AcetylationELGYGDHKPKSSTAA
CCCCCCCCCCCCCHH		59.9026051181
468UbiquitinationELGYGDHKPKSSTAA
CCCCCCCCCCCCCHH		59.90-
468SumoylationELGYGDHKPKSSTAA
CCCCCCCCCCCCCHH		59.90-
472PhosphorylationGDHKPKSSTAAQEVK
CCCCCCCCCHHHHHH		28.3523312004
473PhosphorylationDHKPKSSTAAQEVKT
CCCCCCCCHHHHHHH		32.8623312004
479UbiquitinationSTAAQEVKTLDGIFS
CCHHHHHHHHHCCCC		42.49-
506PhosphorylationIARDESETEKEKIKK
EECCCCHHHHHHHHC		62.7322985185
510UbiquitinationESETEKEKIKKLPEY
CCHHHHHHHHCCCCC		71.53-
513UbiquitinationTEKEKIKKLPEYNPR
HHHHHHHCCCCCCCC		73.14-
513MethylationTEKEKIKKLPEYNPR
HHHHHHHCCCCCCCC		73.1483040029
513AcetylationTEKEKIKKLPEYNPR
HHHHHHHCCCCCCCC		73.1423749302
517PhosphorylationKIKKLPEYNPRTL--
HHHCCCCCCCCCC--		28.6428152594
520MethylationKLPEYNPRTL-----
CCCCCCCCCC-----		45.05115918349
521PhosphorylationLPEYNPRTL------
CCCCCCCCC------		37.7722617229
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of RCC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RCC2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of RCC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRSF5_HUMANSRSF5physical
22939629
VIME_HUMANVIMphysical
22939629
SYMC_HUMANMARSphysical
26344197
RAC1_MOUSERac1physical
25074804
COR1C_HUMANCORO1Cphysical
25074804
IQGA1_HUMANIQGAP1physical
25074804
PK1IP_HUMANPAK1IP1physical
25074804
CDC42_HUMANCDC42physical
25074804
DOC11_HUMANDOCK11physical
25074804
RAC1_HUMANRAC1physical
25074804
PAK4_HUMANPAK4physical
25074804
RGAP1_HUMANRACGAP1physical
25074804
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RCC2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92; LYS-293 AND LYS-377, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-347, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-50 AND SER-51,AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-51, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-44; SER-45;SER-46; SER-50 AND SER-51, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20, AND MASSSPECTROMETRY.

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